A general approach to the study of conformational changes and reactions of nucleic acids and proteins by resonance Raman spectroscopy is outlined. It will permit the study of dilute solutions of biomolecules with concentrations comparable to those used in UV absorption studies. This involves excitation with tunable ultraviolet radiation from a frequency doubled cavity dumped dye laser that is mode locked by synchronously pumping it with a mode locked argon ion laser. Techniques for increasing the power and tuning range of this system are discussed. The nitrogen heterocycles of the nucleic acids and aromatic side chain groups of the proteins serve as the chromophores. Since fluorescence, particularly of trace impurities, becomes more of a problem with excitation in the ultraviolet, a time resolved Raman instrument for rejection of fluorescence is outlined. Factors affecting the signal: noise in the time resolved experiment are outlined, and techniques for increasing the rate at which detected photons can be processed are proposed. To test the extent to which scattering from individual bases of nucleic acid mixtures can be enhanced by proper choice of excitation frequency, we propose to examine first mixtures of mononucleotides with base composition corresponding to native polynucleotides. This will by followed by studies of the melting of penicillium chrysogenum mycophage RNA and calf thymus DNA. Electrophilic attack perturbs the ultraviolet absorption of nucleic acids, and we propose to evaluate the resonance Raman technique for studies of reactions of this type using CH3Hg(II) as a probe ion. To evaluate the extent to which resonsance enhancememt of aromatic side chains in proteins can be obtained we propose to determine th excitation profiles for the amino acids tryptophan, tyrosine, and phenylalanine. To probe the effect of charge and environment, we propose to examine the variation of pH and change of solvent from water, to ethylene glycol. Finally to evaluate the application to reactions of proteins in general, the reversible thermal unfolding of bovine pancreatic ribonuclease A will be studied.